Crystal structure of the carbinolamine intermediate in the reductive half-reaction of aromatic amine dehydrogenase (aadh) with tryptamine. monoclinic form

Structure

x-ray diffraction · 3 distinct chains · 6% helix, 47% strand (DSSP).

Ligands and binding sites

• TSH · 2-(1H-indol-3-yl)ethanimine · ligand · chains D, B
• TSC · (1S)-1-amino-2-(1H-indol-3-yl)ethanol · ligand · chains H, A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• H–A · 1415 Ų buried · 28 hydrogen bonds · protein-protein
• D–B · 1394 Ų buried · 27 hydrogen bonds · protein-protein
• A–B · 925 Ų buried · 19 hydrogen bonds · protein-protein
• D–A · 913 Ų buried · 12 hydrogen bonds · protein-protein
• H–B · 898 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide, 2 covalent, 2 modified (disulfide, covalent ligand, cofactor).

Compared structures

• 2AH0 · Crystal structure of the carbinolamine intermediate in the reductive half-reaction of… · the same entry in another collection · chain B against B, TM-score 1.00
• P84887 · AlphaFold monomer V2.0 prediction for aralkylamine dehydrogenase light chain (P84887) · a predicted model of the same protein · chain H against A, TM-score 1.00
• P84888 · AlphaFold monomer V2.0 prediction for aralkylamine dehydrogenase heavy chain (P84888) · a predicted model of the same protein · chain B against A, TM-score 0.99

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P84887
• Every structure of UniProt P84888
• Elsewhere: RCSB PDB 2AH0 · PDBe 2AH0 · UniProt P84887 · UniProt P84888